STRINGSTRING
Swoo_4516 Swoo_4516 miaB miaB bioB bioB Swoo_3504 Swoo_3504 Swoo_3397 Swoo_3397 pqqE pqqE Swoo_2002 Swoo_2002 Swoo_1999 Swoo_1999 Swoo_0053 Swoo_0053 moaA moaA Swoo_0382 Swoo_0382 Swoo_1222 Swoo_1222 Swoo_1326 Swoo_1326 Swoo_4806 Swoo_4806 moaA-2 moaA-2 lipA lipA
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
Swoo_4516PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB; KEGG: sse:Ssed_0456 radical SAM domain protein. (293 aa)
miaBtRNA-i(6)A37 thiotransferase enzyme MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. (474 aa)
bioBBiotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family. (354 aa)
Swoo_3504PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB; KEGG: spl:Spea_2276 radical SAM domain protein. (646 aa)
Swoo_3397KEGG: spl:Spea_2394 coproporphyrinogen dehydrogenase; PFAM: Radical SAM domain protein; HemN domain protein; SMART: Elongator protein 3/MiaB/NifB. (439 aa)
pqqECoenzyme PQQ biosynthesis protein E; Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ). (371 aa)
Swoo_2002KEGG: spk:MGAS9429_Spy0880 oxygen-independent coproporphyrinogen-III oxidase; TIGRFAM: oxygen-independent coproporphyrinogen III oxidase; PFAM: Radical SAM domain protein; HemN domain protein; SMART: Elongator protein 3/MiaB/NifB. (448 aa)
Swoo_1999PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB; KEGG: gme:Gmet_1693 radical SAM. (506 aa)
Swoo_0053KEGG: sse:Ssed_0090 coproporphyrinogen dehydrogenase; TIGRFAM: oxygen-independent coproporphyrinogen III oxidase; PFAM: Radical SAM domain protein; HemN domain protein; SMART: Elongator protein 3/MiaB/NifB; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (446 aa)
moaAMolybdenum cofactor biosynthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (328 aa)
Swoo_0382PFAM: Radical SAM domain protein; Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB; KEGG: sse:Ssed_4218 radical SAM N-terminal domain protein. (763 aa)
Swoo_1222KEGG: sse:Ssed_1127 conserved hypothetical radical SAM protein; TIGRFAM: conserved hypothetical radical SAM protein; PFAM: Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB. (312 aa)
Swoo_1326Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (378 aa)
Swoo_4806KEGG: sse:Ssed_4414 coproporphyrinogen dehydrogenase; PFAM: Radical SAM domain protein; HemN domain protein; SMART: Elongator protein 3/MiaB/NifB. (445 aa)
moaA-2Molybdenum cofactor biosynthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (326 aa)
lipALipoic acid synthetase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. (321 aa)
Your Current Organism:
Shewanella woodyi
NCBI taxonomy Id: 392500
Other names: S. woodyi ATCC 51908, Shewanella woodyi ATCC 51908, Shewanella woodyi str. ATCC 51908, Shewanella woodyi strain ATCC 51908
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